Chinese Hamster Ovary Cells Selected for Resistance to the Cytotoxicity of Phytohemagglutinin are Deficient in a UDP-N-acetylglucosamine-glycoprotein N-acetylglucosaminyltransferase Activity

Several clones of Chinese hamster ovary cells resistant to the cytotoxicity of the phytohemagglutinin from Phaseolus vulgaris show decreased binding of125I-labeled phytohemagglutinin and contain decreased levels of a UDP-N-acetylglucosamine-glycoprotein N-acetylglucosaminyltransferase (EC 2.4.1.51;...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1975-09, Vol.72 (9), p.3323-3327
Main Authors: Stanley, Pamela, Narasimhan, Saroja, Siminovitch, Louis, Schachter, Harry
Format: Article
Language:English
Subjects:
Binding Sites
Cell extracts
Cell Line
Cell lines
Cell Survival - drug effects
Cells, Cultured - drug effects
Cells, Cultured - enzymology
Cells, Cultured - metabolism
CHO cells
Cytotoxicity
Enzymes
Glucosyltransferases - deficiency
Glucosyltransferases - metabolism
Glycopeptides
Glycoproteins
Kinetics
Lectins
Lectins - pharmacology
Mutation
Phenotypes
Somatic cells
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Summary:Several clones of Chinese hamster ovary cells resistant to the cytotoxicity of the phytohemagglutinin from Phaseolus vulgaris show decreased binding of125I-labeled phytohemagglutinin and contain decreased levels of a UDP-N-acetylglucosamine-glycoprotein N-acetylglucosaminyltransferase (EC 2.4.1.51; UDP-2-acetamido-2-deoxy-D-glucose:glycoprotein 2-acetamido-2-deoxy-D-glucosyltransferase) activity when compared to wild-type cells. The decrease in transferase activity varies from 45% to 96%, depending on the exogenous acceptor used in the enzyme assay. No differences between lectin-resistant and wild-type cells were noted for several other glycosyltransferases. The absence of a particular N-acetylglucosaminyltransferase in the lectin-resistant cells apparently results in defective glycosylation of lectin-binding glycoproteins on the cell surface. A phytohemagglutinin-resistant clone which shows decreased binding of125I-labeled phytohemagglutinin but does not exhibit the enzyme deficiency has also been isolated.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.72.9.3323